TASP1_ARATH
ID TASP1_ARATH Reviewed; 408 AA.
AC O65268;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative threonine aspartase;
DE Short=Taspase-1;
DE EC=3.4.25.-;
DE Contains:
DE RecName: Full=Putative threonine aspartase subunit alpha;
DE Contains:
DE RecName: Full=Putative threonine aspartase subunit beta;
DE Flags: Precursor;
GN OrderedLocusNames=At4g00590; ORFNames=F6N23.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O65268-1; Sequence=Displayed;
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX827980; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80868.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF058919; AAC13614.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80868.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81906.1; -; Genomic_DNA.
DR EMBL; BX827980; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T01223; T01223.
DR RefSeq; NP_191968.3; NM_116284.4. [O65268-1]
DR AlphaFoldDB; O65268; -.
DR SMR; O65268; -.
DR STRING; 3702.AT4G00590.1; -.
DR MEROPS; T02.004; -.
DR PaxDb; O65268; -.
DR PRIDE; O65268; -.
DR EnsemblPlants; AT4G00590.1; AT4G00590.1; AT4G00590. [O65268-1]
DR GeneID; 827968; -.
DR Gramene; AT4G00590.1; AT4G00590.1; AT4G00590. [O65268-1]
DR KEGG; ath:AT4G00590; -.
DR Araport; AT4G00590; -.
DR TAIR; locus:2127068; AT4G00590.
DR eggNOG; KOG1592; Eukaryota.
DR HOGENOM; CLU_021603_5_0_1; -.
DR InParanoid; O65268; -.
DR OMA; RLWCAFT; -.
DR BioCyc; ARA:AT4G00590-MON; -.
DR PRO; PR:O65268; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65268; baseline and differential.
DR Genevisible; O65268; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04514; Taspase1_like; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR InterPro; IPR037464; Taspase1.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autocatalytic cleavage; Hydrolase; Protease;
KW Reference proteome; Threonine protease; Zymogen.
FT CHAIN 1..221
FT /note="Putative threonine aspartase subunit alpha"
FT /id="PRO_0000045448"
FT CHAIN 222..408
FT /note="Putative threonine aspartase subunit beta"
FT /id="PRO_0000045449"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 250..253
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 221..222
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 42626 MW; 027EF45CBD9537EA CRC64;
MMAGDGADQS RRFFVAVHVG AGYHAAANEK ALRSVMRRAC LAASTILRQD SGECIDAVSA
AIQVLEDDPS TNAGRGSNLT EDGHVECDAS LMDGDSGMFG GVGAVPGVRN AIKIAALLVK
EQITGSTLLG RIPPMLLVGE GARRWGKSKS VLIPGTVTEA DQWLVTERAR NQWRRFKAML
SEVGAKSILS AEEHPRGTEN NETCEENVSS CAAADEDKIM DTVGVICVDN EGHIACGSSS
GGIAMKISGR VGLAATYGSG CWASSKGPFG APFLVGCCVS GAGEYLMRGF AARECCTSLA
LSQAGPASAA MKVLRSVMHQ ESSKIGTADK TAGILVVQAD ASVVVPGSKP ELNAVEIAAA
YSSLSFGVGY YGNSIEKPKI SILRTRRQMS EAGVDHFEAR IDLRPTCC
